BMRB

Biological Magnetic Resonance Data Bank


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BMRB Entry 51444

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51444

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Title: Isoleucine d1-methyl chemical shift assignments for FhaC in lipid nanodiscs   PubMed: 35936790

Deposition date: 2022-05-14 Original release date: 2022-06-14

Authors: Sicoli, Giuseppe; Konijnenberg, Albert; Guerin, Jeremy; Hessmann, Steve; Del Nero, Elise; Hernandez-Alba, Oscar; Lecher, Sophie; Rouaut, Guillaume; Muggenburg, Linn; Vezin, Herve; Cianferani, Sarah; Sobott, Frank; Schneider, Robert; Jacob-Dubuisson, Francoise

Citation: Sicoli, Giuseppe; Konijnenberg, Albert; Guerin, Jeremy; Hessmann, Steve; Del Nero, Elise; Hernandez-Alba, Oscar; Lecher, Sophie; Rouaut, Guillaume; Muggenburg, Linn; Vezin, Herve; Cianferani, Sarah; Sobott, Frank; Schneider, Robert; Jacob-Dubuisson, Francoise. "Large-Scale Conformational Changes of FhaC Provide Insights Into the Two-Partner Secretion Mechanism"  Front. Mol. Biosci. 9, 950871-950871 (2022).

Assembly members:
entity_1, polymer, 554 residues, 61345 Da.

Natural source:   Common Name: Bordetella pertussis   Taxonomy ID: 520   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bordetella pertussis

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pT7FcW

Entity Sequences (FASTA):
entity_1: QAQLLPGARDLNRIDDRQRK EQLQRDIERALTRPPVELNP QSEAAAPARKPDATSGHTVT VHAVDLDFGVEGRLFDPAPL VQDYLNRPLDNEQLFLLVKA LSAALYDRGYATSIVTFVPP GVVDGVLKLKVEWGRIKGWL IDGKPLEGTRDRMMVFSAMP GWQDKVLNVFDIDQAIYNIN NGGKTGNITIVPADEYGYSY LDLQLQRRALPRVSLGMDNS GPGTPENGRYKYNASVTAND LLGLNDTLGLYIGNRYYRDA GHDAERNYDLMYSVPLGRTR LDLQTGYSTYRNLLKTRYGQ YQSAGNSRSFGLKATRLLYR DTRSQFSVYGGLKLRQNKNY LAGTRLDVSSKHYSDVTVGM QYSTQRGANAYFGDLSFTRG VGVNNGKYAAYDERGPQGNV SRFNGSLAWTRYMALAGQPI QWASQLGFQYSRQQLLNSYQ ITVGDEYTVRGYNLRTSQSG DSGVYLSNTLTVPVQFSLLG KQASVAPFVGADVGALKSNH PDARTIRMAGLAAGVRFDLP YARMSFTYSKPVGAQPGGAP RAPVWLYINAGLSF

Data sets:
Data typeCount
13C chemical shifts15
1H chemical shifts45

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1FhaC1

Entities:

Entity 1, FhaC 554 residues - 61345 Da.

1   GLNALAGLNLEULEUPROGLYALAARGASP
2   LEUASNARGILEASPASPARGGLNARGLYS
3   GLUGLNLEUGLNARGASPILEGLUARGALA
4   LEUTHRARGPROPROVALGLULEUASNPRO
5   GLNSERGLUALAALAALAPROALAARGLYS
6   PROASPALATHRSERGLYHISTHRVALTHR
7   VALHISALAVALASPLEUASPPHEGLYVAL
8   GLUGLYARGLEUPHEASPPROALAPROLEU
9   VALGLNASPTYRLEUASNARGPROLEUASP
10   ASNGLUGLNLEUPHELEULEUVALLYSALA
11   LEUSERALAALALEUTYRASPARGGLYTYR
12   ALATHRSERILEVALTHRPHEVALPROPRO
13   GLYVALVALASPGLYVALLEULYSLEULYS
14   VALGLUTRPGLYARGILELYSGLYTRPLEU
15   ILEASPGLYLYSPROLEUGLUGLYTHRARG
16   ASPARGMETMETVALPHESERALAMETPRO
17   GLYTRPGLNASPLYSVALLEUASNVALPHE
18   ASPILEASPGLNALAILETYRASNILEASN
19   ASNGLYGLYLYSTHRGLYASNILETHRILE
20   VALPROALAASPGLUTYRGLYTYRSERTYR
21   LEUASPLEUGLNLEUGLNARGARGALALEU
22   PROARGVALSERLEUGLYMETASPASNSER
23   GLYPROGLYTHRPROGLUASNGLYARGTYR
24   LYSTYRASNALASERVALTHRALAASNASP
25   LEULEUGLYLEUASNASPTHRLEUGLYLEU
26   TYRILEGLYASNARGTYRTYRARGASPALA
27   GLYHISASPALAGLUARGASNTYRASPLEU
28   METTYRSERVALPROLEUGLYARGTHRARG
29   LEUASPLEUGLNTHRGLYTYRSERTHRTYR
30   ARGASNLEULEULYSTHRARGTYRGLYGLN
31   TYRGLNSERALAGLYASNSERARGSERPHE
32   GLYLEULYSALATHRARGLEULEUTYRARG
33   ASPTHRARGSERGLNPHESERVALTYRGLY
34   GLYLEULYSLEUARGGLNASNLYSASNTYR
35   LEUALAGLYTHRARGLEUASPVALSERSER
36   LYSHISTYRSERASPVALTHRVALGLYMET
37   GLNTYRSERTHRGLNARGGLYALAASNALA
38   TYRPHEGLYASPLEUSERPHETHRARGGLY
39   VALGLYVALASNASNGLYLYSTYRALAALA
40   TYRASPGLUARGGLYPROGLNGLYASNVAL
41   SERARGPHEASNGLYSERLEUALATRPTHR
42   ARGTYRMETALALEUALAGLYGLNPROILE
43   GLNTRPALASERGLNLEUGLYPHEGLNTYR
44   SERARGGLNGLNLEULEUASNSERTYRGLN
45   ILETHRVALGLYASPGLUTYRTHRVALARG
46   GLYTYRASNLEUARGTHRSERGLNSERGLY
47   ASPSERGLYVALTYRLEUSERASNTHRLEU
48   THRVALPROVALGLNPHESERLEULEUGLY
49   LYSGLNALASERVALALAPROPHEVALGLY
50   ALAASPVALGLYALALEULYSSERASNHIS
51   PROASPALAARGTHRILEARGMETALAGLY
52   LEUALAALAGLYVALARGPHEASPLEUPRO
53   TYRALAARGMETSERPHETHRTYRSERLYS
54   PROVALGLYALAGLNPROGLYGLYALAPRO
55   ARGALAPROVALTRPLEUTYRILEASNALA
56   GLYLEUSERPHE

Samples:

sample_1: FhaC, [U-2H; U-15N; U-(13CD,1HD)Ile], 90 uM; MSP1D1, [U-2H], 270 uM; DMPC, [U-2H], 11.3 mM; DMPG, [U-2H], 4.9 mM; DSS 140 uM; sodium phosphate 100 mM

sample_2: FhaC I176V, [U-2H; U-15N; U-(13CD,1HD)Ile], 56 uM; MSP1D1, [U-2H], 168 uM; DMPC, [U-2H], 7.0 mM; DMPG, [U-2H], 3.0 mM; DSS 140 uM; sodium phosphate 50 mM

sample_3: FhaC I176V, [U-2H; U-15N; U-(13CD,1HD)Ile], 56 uM; MSP1D1, [U-2H], 168 uM; DMPC, [U-2H], 7.0 mM; DMPG, [U-2H], 3.0 mM; DSS 140 uM; sodium phosphate 50 mM

sample_4: FhaC C195-MTSL, [U-2H; U-15N; U-(13CD,1HD)Ile], 90 uM; MSP1D1, [U-2H], 270 uM; DMPC, [U-2H], 11.3 mM; DMPG, [U-2H], 4.9 mM; DSS 140 uM; sodium phosphate 50 mM

sample_5: FhaC C195-MTSL, [U-2H; U-15N; U-(13CD,1HD)Ile], 88 uM; MSP1D1, [U-2H], 265 uM; DMPC, [U-2H], 11.1 mM; DMPG, [U-2H], 4.8 mM; DSS 137 uM; sodium phosphate 50 mM; ascorbate 880 uM

sample_conditions_1: ionic strength: 50 mM; pH*: 7.2; pressure: 1 atm; temperature: 305 K

sample_conditions_2: ionic strength: 100 mM; pH*: 7.2; pressure: 1 atm; temperature: 305 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-13C HMQCsample_1isotropicsample_conditions_1
2D 1H-13C HMQCsample_1isotropicsample_conditions_2
2D 1H-13C HMQCsample_4isotropicsample_conditions_1
2D 1H-13C HMQCsample_5isotropicsample_conditions_1
2D 1H-13C SOFAST-HMQCsample_2isotropicsample_conditions_1
2D 1H-13C SOFAST-HMQCsample_3isotropicsample_conditions_1

Software:

TOPSPIN v4.0.3 - collection, processing

NMRPipe v10.6 - processing

NMRFAM-SPARKY v1.4 - chemical shift assignment, data analysis, peak picking

CcpNMR v2.4.2 - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker AVANCE NEO 900 MHz

Related Database Links:

PDB
UniProt P35077
AlphaFold P35077